Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15

被引：60
作者：
Cheng, LM
Tachibana, K
Iwasaki, H
Kameyama, A
Zhang, Y
Kubota, T
Hiruma, T
Tachibana, K
Kudo, T
Guo, JM
Narimatsu, H
机构：
[1] AIST, Res Ctr Glycosci, Glycogene Funct Team, Tsukuba, Ibaraki 3058568, Japan
[2] Amerham Biosci KK, Shinjuku Ku, Tokyo 1690073, Japan
[3] Fujirebio Inc, Diagnost Res Labs, Tokyo 1920031, Japan
来源：
FEBS LETTERS | 2004年 / 566卷 / 1-3期
关键词：
UDP-GaINAc : polypeptide; N-acetylgalactosaminyltransferase (EC 2.4.1.41); O-glycosylation; O-glycan; mucin;
D O I：
10.1016/j.febslet.2004.03.108
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
We have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：17 / 24
页数：8
相关论文
共 38 条
[1]  
ALBONE EF, 1994, J BIOL CHEM, V269, P16845
[2]   The AATPAP sequence is a very efficient signal for O-glycosylation in CHO cells [J].
Asada, M ;
Orikasa, N ;
Yoneda, A ;
Oda, Y ;
Ota, K ;
Imamura, T .
GLYCOCONJUGATE JOURNAL, 1999, 16 (07) :321-326
[3]   cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine - Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3 [J].
Bennett, EP ;
Hassan, H ;
Clausen, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (29) :17006-17012
[4]   Cloning of a human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat [J].
Bennett, EP ;
Hassan, H ;
Mandel, U ;
Mirgorodskaya, E ;
Roepstorff, P ;
Burchell, J ;
Taylor-Papadimitriou, J ;
Hollingsworth, MA ;
Merkx, G ;
van Kessel, AG ;
Eiberg, H ;
Steffensen, R ;
Clausen, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (46) :30472-30481
[5]   Cloning and characterization of a close homologue of human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6 -: Evidence for genetic but not functional redundancy [J].
Bennett, EP ;
Hassan, H ;
Mandel, U ;
Hollingsworth, MA ;
Akisawa, N ;
Ikematsu, Y ;
Merkx, G ;
van Kessel, AG ;
Olofsson, S ;
Clausen, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (36) :25362-25370
[6]   A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates [J].
Bennett, EP ;
Hassan, H ;
Hollingsworth, MA ;
Clausen, H .
FEBS LETTERS, 1999, 460 (02) :226-230
[7]   Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10 [J].
Cheng, LM ;
Tachibana, K ;
Zhang, Y ;
Guo, J ;
Tachibana, KK ;
Kameyama, A ;
Wang, H ;
Hiruma, T ;
Iwasaki, H ;
Togayachi, A ;
Kudo, T ;
Narimatsu, H .
FEBS LETTERS, 2002, 531 (02) :115-121
[8]   CHARACTERIZATION OF THE HUMAN MUCIN GENE MUC5AC - A CONSENSUS CYSTEINE-RICH DOMAIN FOR 11P15 MUCIN GENES [J].
DUPERAT, VG ;
AUDIE, JP ;
DEBAILLEUL, V ;
LAINE, A ;
BUISINE, MP ;
GALIEGUEZOUITINA, S ;
PIGNY, P ;
DEGAND, P ;
AUBERT, JP ;
PORCHET, N .
BIOCHEMICAL JOURNAL, 1995, 305 :211-219
[9]   The acceptor specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases [J].
Elhammer, ÅP ;
Kézdy, FJ ;
Kurosaka, A .
GLYCOCONJUGATE JOURNAL, 1999, 16 (02) :171-180
[10]  
GENDLER SJ, 1990, J BIOL CHEM, V265, P15286
1234